Caspase-8 also known as MCH5, CASP8 is a member of the cysteine-aspartic acid protease (caspase) family. Caspase-8 plays a crucial role in the apoptotic signaling pathway, acting as an initiator caspase that activates downstream effector caspases through the cleavage of their inactive precursors. This process is vital for the regulation of programmed cell death, particularly in response to death receptor signaling via tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and Fas (TNFRSF6). Caspase-8 is primarily located in the cytoplasm and is recruited to the death-inducing signaling complex (DISC) upon binding to the adaptor molecule FADD, where activation occurs. The active form of caspase-8, a heterodimer composed of p18 and p10 subunits, is then released from the DISC to propagate the apoptotic signal.